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Literature summary for 1.3.1.34 extracted from

  • Hubbard, P.A.; Liang, X.; Schulz, H.; Kim, J.J.
    The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase (2003), J. Biol. Chem., 278, 37553-37560.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme is a iron-sulfur flavoenzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from strain BL21(DE3) via DEAE ion exchange and affinity chromatography Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+ reaction mechanism, active site structure, substrate binding site, His252 is the catalytic residue Escherichia coli

Synonyms

Synonyms Comment Organism
2,4-dienoyl-CoA reductase
-
Escherichia coli
DCR
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
flavin enzyme is a iron-sulfur flavoenzyme Escherichia coli